Degradation of vitronectin by matrix metalloproteinases‐1, ‐2, ‐3, ‐7 and ‐9

FEBS Letters

Shikata, Hideo²  Imai, Kazushi¹  Okada, Yasunori¹ 

[1] Department of Molecular Immunology and Pathology, Cancer Research Institute, Kanazawa University, 13-1 Takara-machi, Kanazawa, Ishikawa 920, Japan;Department of Oral Pathology, School of Dentistry, Meikai University, Sakado, Saitama 350-02, Japan

关键词: Vitronectin;    Matrix metalloproteinase;    Degradation;    Kinetics;   

DOI  :  10.1016/0014-5793(95)00752-U

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The susceptibility of vitronectin (Vn) purified from human plasma to digestion by matrix metalloproteinases (MMPs) was examined. MMP-2, -3, -7 and -9 except for MMP-1 degraded Vn into multiple fragments. MMP-7 showed the highest activity to the substrate among these MMPs, digesting 8-, 30- and 44-fold more preferentially than MMP-2, -3 and -9, respectively. These data suggest that MMP-2, -3, -7 and -9 may be responsible for the pathological degradation and/or normal turnover of Vn.

【 授权许可】

Unknown